N-terminal truncation of a maleate cis-trans isomerase from Rhodococcus jostii RHA1 results in a highly active enzyme for the biocatalytic production of fumaric acid
文献类型：期刊论文
| 作者 | Liu, Xiangtao; Zhao, Qing; Ren, Jie; Dong, Wenyue; Wu, Qiaqing; Zhu, Dunming |
| 刊名 | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
 |
| 出版日期 | 2013-09-01 |
| 卷号 | 93页码:44-50 |
| 关键词 | Rhodococcus jostii Maleate cis-trans isomerase Fumaric acid Biocatalytic isomerization |
| 英文摘要 | As part of the project to develop an efficient biocatalytic process for the production of fumaric acid, a full-length putative maleate cis-trans isomerase gene from Rhodococcus jostii RHA1 was synthesized and expressed in Escherichia coil Rosetta2 (DE3) pLysS, but the protein was not soluble and showed no catalytic activity. Bioinformatics analysis of the protein sequence indicated that there were two hydrophilic and two hydrophobic amino acid clusters in an alternate arrangement at the N-terminus, and 50 extra amino acid residues at the N-terminus were not present in the known maleate cis-trans isomerases. The alternate hydrophilic and hydrophobic clusters at the N-terminus were thus truncated one by one to evaluate their effect on the gene expression and enzyme activity. Three mutants (MaiR-D41/42-304AA, MaiR-D48/49-304AA and MaiR-D52/53-304AA) without the hydrophilic and hydrophobic clusters were expressed as soluble protein with maleate cis-trans isomerase activity. Among them, MaiR-D48 was purified and its properties were studied. The purified enzyme had a temperature optimum of 40 degrees C and a wide pH range (5.0-9.0) with the optimum pH being 8.0: The whole cells of E. coil expressing MaiR-D48 catalyzed the isomerization of maleic acid to fumaric acid at I M substrate concentration, showing its potential for industrial use. (C) 2013 Elsevier B.V. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
| 类目[WOS] | Biochemistry & Molecular Biology ; Chemistry, Physical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
| 关键词[WOS] | TRANSFORMATION ; GENE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000321173300007 |
| 源URL | [http://124.16.173.210/handle/834782/1259]  |
| 专题 | 天津工业生物技术研究所_生物催化与绿色化工 朱敦明_期刊论文 |
| 作者单位 | Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Lab Ind Enzymes, Tianjin Airport Econ Area, Tianjin 300308, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Xiangtao,Zhao, Qing,Ren, Jie,et al. N-terminal truncation of a maleate cis-trans isomerase from Rhodococcus jostii RHA1 results in a highly active enzyme for the biocatalytic production of fumaric acid[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2013,93:44-50. |
| APA | Liu, Xiangtao,Zhao, Qing,Ren, Jie,Dong, Wenyue,Wu, Qiaqing,&Zhu, Dunming.(2013).N-terminal truncation of a maleate cis-trans isomerase from Rhodococcus jostii RHA1 results in a highly active enzyme for the biocatalytic production of fumaric acid.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,93,44-50. |
| MLA | Liu, Xiangtao,et al."N-terminal truncation of a maleate cis-trans isomerase from Rhodococcus jostii RHA1 results in a highly active enzyme for the biocatalytic production of fumaric acid".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 93(2013):44-50. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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